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CSIRO, Division of Protein Chemistry, Parkville, 3052, Victoria, Australia
The amino acid sequence of the Hong Kong haemagglutinin light chain (HA2; 222 residues) is nearly complete, lacking only the definition of a highly aggregated region near the carboxyl terminal end of the chain. This unsequenced area of approx. 25 residues occurs near the carboxyl terminal end of cyanogen bromide peptide CN-1, whose structure determination is discussed in this paper. All
-cystine residues present in HA2 occur in CN-1, as a proximal cluster involving residues 137, 144 and 148, and as a distal cluster involving four other
-cystine residues near the carboxyl terminus of HA2, three of which have been placed within peptides. The single glycosylated asparagine in HA2 also occurs in CN-1; the carbohydrate moiety is complex. The structure of HA2 is discussed in terms of its properties, and compared with published data from haemagglutinins from other influenza strains.
Received 26 March 1980;
accepted 19 May 1980.
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